Sandbox GGC4: Difference between revisions
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Apolipoprotein a-1 (apoA-I) is a fairly small molecule that consists of a total of 243 residues and is 29-kD polypeptide in size. Its structure consists of two helical domains that include a four-helix of antiparallel bundle by N terminal and two helix bundle at the C terminal end. ApoA-I consists of <scene name='75/752268/Chains/1'>four chains</scene> alpha helices including chain A (orange), B (blue), C (red), and D (green) as displayed, in which an infinity like structure. C terminal domain of carboxyl group is known to participate in role in lipid binding for transport, found following between residues <scene name='75/752268/Cterm_binding/1'>(190-243).</scene> | Apolipoprotein a-1 (apoA-I) is a fairly small molecule that consists of a total of 243 residues and is 29-kD polypeptide in size. Its structure consists of two helical domains that include a four-helix of antiparallel bundle by N terminal and two helix bundle at the C terminal end. ApoA-I consists of <scene name='75/752268/Chains/1'>four chains</scene> alpha helices including chain A (orange), B (blue), C (red), and D (green) as displayed, in which an infinity like structure. C terminal domain of carboxyl group is known to participate in role in lipid binding for transport, found following between residues <scene name='75/752268/Cterm_binding/1'>(190-243).</scene> | ||
Apolipoprotein a-1 in the monomer form truncated (lacking 1-43 residues) consists of unique pseudo-continuous alpha helix highlighted by kinks at <scene name='75/752268/Truncated/3'>Pro residues</scene>, spaced approximately every 22 residues.<ref>Nagao, K., Hata, M., Tanaka, K., Takechi, Y., Nguyen, D., Dhanasekaran, P., . . . Saito, H. (2014, January). The roles of C-terminal helices of human apolipoprotein A-I in formation of high-density lipoprotein particles. Retrieved November 14, 2020, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3863607/</ref> | Apolipoprotein a-1 in the monomer form <scene name='75/752268/Truncated/4'>truncated</scene> (lacking 1-43 residues) consists of unique pseudo-continuous alpha helix highlighted by kinks at <scene name='75/752268/Truncated/3'>Pro residues</scene>, spaced approximately every 22 residues.<ref>Nagao, K., Hata, M., Tanaka, K., Takechi, Y., Nguyen, D., Dhanasekaran, P., . . . Saito, H. (2014, January). The roles of C-terminal helices of human apolipoprotein A-I in formation of high-density lipoprotein particles. Retrieved November 14, 2020, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3863607/</ref> | ||
